P56528 · CD38_MOUSE
- ProteinADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 1
- GeneCd38
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids304 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Synthesizes the second messengers cyclic ADP-ribose (cADPR) and nicotinate-adenine dinucleotide phosphate (NAADP), the former a second messenger for glucose-induced insulin secretion, the latter a Ca2+ mobilizer (PubMed:11829748).
Also has cADPR hydrolase activity (By similarity).
Also has cADPR hydrolase activity (By similarity).
Catalytic activity
- NAD+ = cyclic ADP-beta-D-ribose + H+ + nicotinamide
Features
Showing features for active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 123 | |||||
Sequence: C | ||||||
Active site | 205 | |||||
Sequence: C |
GO annotations
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 1
- EC number
- Alternative names
- CD Antigen Name
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionP56528
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Membrane ; Single-pass type II membrane protein
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-21 | Cytoplasmic | ||||
Sequence: MANYEFSQVSGDRPGCRLSRK | ||||||
Transmembrane | 22-44 | Helical; Signal-anchor for type II membrane protein | ||||
Sequence: AQIGLGVGLLVLIALVVGIVVIL | ||||||
Topological domain | 45-304 | Extracellular | ||||
Sequence: LRPRSLLVWTGEPTTKHFSDIFLGRCLIYTQILRPEMRDQNCQEILSTFKGAFVSKNPCNITREDYAPLVKLVTQTIPCNKTLFWSKSKHLAHQYTWIQGKMFTLEDTLLGYIADDLRWCGDPSTSDMNYVSCPHWSENCPNNPITVFWKVISQKFAEDACGVVQVMLNGSLREPFYKNSTFGSVEVFSLDPNKVHKLQAWVMHDIEGASSNACSSSSLNELKMIVQKRNMIFACVDNYRPARFLQCVKNPEHPSCRLNT |
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
Loss of cADPR and NAADP synthesis.
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 16 variants from UniProt as well as other sources including ClinVar and dbSNP.
Chemistry
PTM/Processing
Features
Showing features for chain, disulfide bond, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000144068 | 1-304 | ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 1 | |||
Sequence: MANYEFSQVSGDRPGCRLSRKAQIGLGVGLLVLIALVVGIVVILLRPRSLLVWTGEPTTKHFSDIFLGRCLIYTQILRPEMRDQNCQEILSTFKGAFVSKNPCNITREDYAPLVKLVTQTIPCNKTLFWSKSKHLAHQYTWIQGKMFTLEDTLLGYIADDLRWCGDPSTSDMNYVSCPHWSENCPNNPITVFWKVISQKFAEDACGVVQVMLNGSLREPFYKNSTFGSVEVFSLDPNKVHKLQAWVMHDIEGASSNACSSSSLNELKMIVQKRNMIFACVDNYRPARFLQCVKNPEHPSCRLNT | ||||||
Disulfide bond | 70↔86 | |||||
Sequence: CLIYTQILRPEMRDQNC | ||||||
Disulfide bond | 103↔184 | |||||
Sequence: CNITREDYAPLVKLVTQTIPCNKTLFWSKSKHLAHQYTWIQGKMFTLEDTLLGYIADDLRWCGDPSTSDMNYVSCPHWSENC | ||||||
Glycosylation | 104 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 124 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 164↔177 | |||||
Sequence: CGDPSTSDMNYVSC | ||||||
Glycosylation | 213 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 223 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 258↔279 | |||||
Sequence: CSSSSLNELKMIVQKRNMIFAC | ||||||
Disulfide bond | 291↔300 | |||||
Sequence: CVKNPEHPSC |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Gene expression databases
Interaction
Subunit
Homodimer.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P56528 | Cd38 P56528 | 5 | EBI-8401721, EBI-8401721 |
Protein-protein interaction databases
Chemistry
Miscellaneous
Structure
Sequence
- Sequence statusComplete
- Length304
- Mass (Da)34,408
- Last updated2004-11-23 v2
- ChecksumDD0A7747C5F67D6F
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 191 | in Ref. 1; AAA03163 | ||||
Sequence: V → M | ||||||
Sequence conflict | 229 | in Ref. 1; AAA03163 | ||||
Sequence: V → L |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
L11332 EMBL· GenBank· DDBJ | AAA03163.1 EMBL· GenBank· DDBJ | mRNA | ||
AK038439 EMBL· GenBank· DDBJ | BAC30000.1 EMBL· GenBank· DDBJ | mRNA | ||
AK040498 EMBL· GenBank· DDBJ | BAC30607.1 EMBL· GenBank· DDBJ | mRNA | ||
AK042970 EMBL· GenBank· DDBJ | BAC31423.1 EMBL· GenBank· DDBJ | mRNA | ||
BC046312 EMBL· GenBank· DDBJ | AAH46312.1 EMBL· GenBank· DDBJ | mRNA |